ID A0A0H3GN18_KLEPH Unreviewed; 571 AA.
AC A0A0H3GN18;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=KPHS_07390 {ECO:0000313|EMBL:AEW59437.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW59437.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW59437.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW59437.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP003200; AEW59437.1; -; Genomic_DNA.
DR RefSeq; WP_004147007.1; NC_016845.1.
DR RefSeq; YP_005225039.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GN18; -.
DR STRING; 1125630.KPHS_07390; -.
DR GeneID; 11845729; -.
DR KEGG; kpm:KPHS_07390; -.
DR PATRIC; fig|1125630.4.peg.719; -.
DR HOGENOM; CLU_020211_11_2_6; -.
DR Proteomes; UP000007841; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16915; HATPase_DpiB-CitA-like; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEW59437.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 48..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 371..566
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 571 AA; 64308 MW; FA41A542450C3377 CRC64;
MSEIFCSVLH LSAPGAQNGE NNNLMSIYPM YTRKITHWFA RRSFQNRIFL LILFTSTIVM
LAMSWYLTDI TEERLHYQVG QRALIQAMQI SAMPELVEAV QKRDLARIKA LIDPMRSFSD
ATYITVGDAS GQRLYHVNPD EIGKSMEGGD SDEALINAKS YVSVRKGSLG SSLRGKSPIQ
DATGKVIGIV SVGYTIEQLE NWLSLQISSL LIPMAIMLLL LLFCARRFSL HIKKQMLNME
PQQLSQLLIQ QSVLFESVFE GLIAIDSDYK ITAINQTARR LLNLSQPEPT LIGKRISSVI
SQEVFFYDAP QTNKKDEIVT FNQIKVIASR MAVILNNEPQ GWVISFRSKD DINTLSLQLS
QVQQYADNLR AVQHEHRNLI STIAGLLFLK RYNQALELIQ QQSESHQKVI DFIARNFQDN
HLAGLLIGKY YRAKELGLEL IFDPACFVDR LPTALSHNEW ISIVGNLLDN AYNASLRQPQ
GSKQIECLIN SDGQEVIIEI ADQGCGIDEA LRDRIFERGV TSSASKDHGI GLWLVRSYVE
QAGGSIVVEN NIPFGTIFTL YIPLTRDEHH G
//